Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RnrL

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulationi

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site (By similarity).By similarity

Pathwayi: DNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei16Allosteric activatorBy similarity1
Binding sitei64Allosteric activatorBy similarity1
Binding sitei99Allosteric activatorBy similarity1
Binding sitei213SubstrateBy similarity1
Sitei229Important for hydrogen atom transferBy similarity1
Sitei237Allosteric effector binding, determines substrate specificityBy similarity1
Binding sitei258Substrate; via amide nitrogenBy similarity1
Sitei267Allosteric effector binding, determines substrate specificityBy similarity1
Active sitei438Proton acceptorBy similarity1
Active sitei440Cysteine radical intermediateBy similarity1
Active sitei442Proton acceptorBy similarity1
Sitei455Important for hydrogen atom transferBy similarity1
Sitei748Important for electron transferBy similarity1
Sitei749Important for electron transferBy similarity1
Sitei807Interacts with thioredoxin/glutaredoxinBy similarity1
Sitei810Interacts with thioredoxin/glutaredoxinBy similarity1

GO - Molecular functioni

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: FlyBase
  • deoxyribonucleotide biosynthetic process Source: UniProtKB
  • DNA replication Source: UniProtKB-UniPathway
  • tissue regeneration Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleoside-diphosphate reductase subunit M1
Ribonucleotide reductase large subunit
Gene namesi
Name:RnrL
ORF Names:CG5371
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0011703. RnrL.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001871931 – 812Ribonucleoside-diphosphate reductase large subunitAdd BLAST812

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi229 ↔ 455Redox-activeBy similarity
Modified residuei778Phosphothreonine1 Publication1
Modified residuei782Phosphoserine1 Publication1
Modified residuei786Phosphotyrosine1 Publication1

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP48591.
PRIDEiP48591.

PTM databases

iPTMnetiP48591.

Expressioni

Gene expression databases

BgeeiFBgn0011703.
GenevisibleiP48591. DM.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Protein-protein interaction databases

BioGridi60477. 3 interactors.
DIPiDIP-19582N.
MINTiMINT-829510.
STRINGi7227.FBpp0079648.

Structurei

3D structure databases

ProteinModelPortaliP48591.
SMRiP48591.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 103ATP-conePROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 28Allosteric activator bindingBy similarity7
Regioni228 – 229Substrate bindingBy similarity2
Regioni296 – 299Allosteric effector binding, determines substrate specificityBy similarity4
Regioni438 – 442Substrate bindingBy similarity5
Regioni614 – 618Substrate bindingBy similarity5

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1112. Eukaryota.
COG0209. LUCA.
GeneTreeiENSGT00390000001372.
InParanoidiP48591.
KOiK10807.
OMAiKMTEIPD.
OrthoDBiEOG091G01XV.
PhylomeDBiP48591.

Family and domain databases

InterProiIPR005144. ATP-cone_dom.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48591-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKNKSMKTS KLYVIKRDGR QEEVHFDKIT SRIQKLCYNL NMDFVDPVTI
60 70 80 90 100
TLQVINGLYC GVTTQELDNL AAEIAAGLTC NHPDYAILAA RIAVSNLHKE
110 120 130 140 150
TKKAFSDVFE DLYNHVNKET NQKVPLVSEF HYNVVKKNAT RLNSSIIYDR
160 170 180 190 200
DFGYNYFGFK TLERSYLLKR NGKIAERPQH MLMRVAIGIH GEDIDAAVET
210 220 230 240 250
YNLLSERYFT HASPTLFAAA TNRPQLSSCF LLTMTADSIE GIFKSVEQCA
260 270 280 290 300
MISKSAGGIG LNVHCIRAKG TSICGTNGTS NGLVPMLRVF NNVARYVDQG
310 320 330 340 350
GGKRPGAFAI YLEPWHSDVF EFLELKKNTG KEENRARDLF YALWIPDLFM
360 370 380 390 400
KRVEANGDWS LMCPHKCPGL HDVWGDEFEK LYEKYEQEGR ANRTVKAQSL
410 420 430 440 450
WFAIIEAQVE TGNPYMLFKD ACNRKSNQQN VGTIKCSNLC TEIVEYSAPD
460 470 480 490 500
EIAVCNLASI ALNMFVTPEK TYDFKKLKEV TKIVTKNLNK IIDINYYPLP
510 520 530 540 550
EARKSNLRHR PVGIGIQGFA DALILMRFPY ESEEAGLLNQ QIFETIYYGA
560 570 580 590 600
LEASCELAQT EGPYETYEGS PVSKGILQYD MWDKVPTNLW DWQKLKESIR
610 620 630 640 650
MHGVRNSLLV APMPTASTAQ IMGNNESFEP YTTNIYTRRV LSGEFQVVNH
660 670 680 690 700
HLLRDLTELD LWDDDMKNQI ISSRGSIQNI ETIPPKVRDL YKTVWEISVK
710 720 730 740 750
STIKMAADRG AFIDQSQSFN IHVAEPNYGK LTSIHFYSWK AGLKTGMYYL
760 770 780 790 800
RTKPAANAIQ FTVNKKQGAV SMNGQNGTAE GSPQKYEEDR ERKMADMVCS
810
LENKDACMSC GS
Length:812
Mass (Da):91,978
Last modified:December 1, 2000 - v2
Checksum:i6E4FC608AC04A5FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF52913.2.
AF132143 mRNA. Translation: AAD33590.1.
AY119149 mRNA. Translation: AAM51009.1.
U09369 Genomic DNA. Translation: AAA56995.1.
RefSeqiNP_477027.1. NM_057679.5.
UniGeneiDm.3216.

Genome annotation databases

EnsemblMetazoaiFBtr0080059; FBpp0079648; FBgn0011703.
GeneIDi34392.
KEGGidme:Dmel_CG5371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF52913.2.
AF132143 mRNA. Translation: AAD33590.1.
AY119149 mRNA. Translation: AAM51009.1.
U09369 Genomic DNA. Translation: AAA56995.1.
RefSeqiNP_477027.1. NM_057679.5.
UniGeneiDm.3216.

3D structure databases

ProteinModelPortaliP48591.
SMRiP48591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60477. 3 interactors.
DIPiDIP-19582N.
MINTiMINT-829510.
STRINGi7227.FBpp0079648.

PTM databases

iPTMnetiP48591.

Proteomic databases

PaxDbiP48591.
PRIDEiP48591.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080059; FBpp0079648; FBgn0011703.
GeneIDi34392.
KEGGidme:Dmel_CG5371.

Organism-specific databases

CTDi34392.
FlyBaseiFBgn0011703. RnrL.

Phylogenomic databases

eggNOGiKOG1112. Eukaryota.
COG0209. LUCA.
GeneTreeiENSGT00390000001372.
InParanoidiP48591.
KOiK10807.
OMAiKMTEIPD.
OrthoDBiEOG091G01XV.
PhylomeDBiP48591.

Enzyme and pathway databases

UniPathwayiUPA00326.

Miscellaneous databases

GenomeRNAii34392.
PROiP48591.

Gene expression databases

BgeeiFBgn0011703.
GenevisibleiP48591. DM.

Family and domain databases

InterProiIPR005144. ATP-cone_dom.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRIR1_DROME
AccessioniPrimary (citable) accession number: P48591
Secondary accession number(s): Q9UB08, Q9VKZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 1, 2000
Last modified: November 30, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.